Member database | PROSITE patterns |
PROSITE patterns type | conserved site |
Short name | TRANSALDOLASE_1 |
Description
Transaldolase (EC 2.2.1.2) catalyzes the reversible transfer of a three-carbon
ketol unit from sedoheptulose 7-phosphate to glyceraldehyde 3-phosphate to
form erythrose 4-phosphate and fructose 6-phosphate. This enzyme, together
with transketolase, provides a link between the glycolytic and pentose-
phosphate pathways. Transaldolase is an enzyme of about 34 Kd whose sequence
has been well conserved throughout evolution. A lysine has been implicated
[2]
in the catalytic mechanism of the enzyme; it acts as a nucleophilic group that
attacks the carbonyl group of fructose-6-phosphate.
Transaldolase is evolutionary related
[1] to a bacterial protein of about 20
Kd (known as talC in Escherichia coli), whose exact function is not yet known.
We developed two signature patterns for these proteins. The first, located in
the N-terminal section, contains a perfectly conserved pentapeptide; the
second, includes the active site lysine.
References
1.Novel phosphotransferase system genes revealed by bacterial genome analysis--a gene cluster encoding a unique Enzyme I and the proteins of a fructose-like permease system. Reizer J, Reizer A, Saier MH Jr. Microbiology (Reading, Engl.) 141 ( Pt 4), 961-71, (1995). PMID: 7773398
2.Lysine144 is essential for the catalytic activity of Saccharomyces cerevisiae transaldolase. Miosga T, Schaaff-Gerstenschlager I, Franken E, Zimmermann FK. Yeast 9, 1241-9, (1993). View articlePMID: 8109173